๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Cold denaturation of ubiquitin

โœ Scribed by Beatriz Ibarra-Molero; George I. Makhatadze; Jose M. Sanchez-Ruiz


Book ID
114149840
Publisher
Elsevier Science
Year
1999
Tongue
English
Weight
245 KB
Volume
1429
Category
Article
ISSN
0167-4838

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Cold Denaturation of Encapsulated Ubiqui
โœ Pometun, Maxim S.; Peterson, Ronald W.; Babu, Charles R.; Wand, A. Joshua ๐Ÿ“‚ Article ๐Ÿ“… 2006 ๐Ÿ› American Chemical Society ๐ŸŒ English โš– 114 KB
Cold denaturation of ubiquitin at high p
โœ Ryo Kitahara; Akira Okuno; Minoru Kato; Yoshihiro Taniguchi; Shigeyuki Yokoyama; ๐Ÿ“‚ Article ๐Ÿ“… 2006 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 827 KB

Cold-induced conformational transition of ubiquitin was studied at pH 4.5 under a constant pressure of 2 kbar using variable pressure one-dimensional 1H and two-dimensional 15N/1H NMR spectroscopy as well as IR spectroscopy. Although a tendency for preferential stabilization of a peculiar locally di

Cold Denaturation of CheY
โœ Gregory T. DeKoster; Andrew D. Robertson ๐Ÿ“‚ Article ๐Ÿ“… 1995 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 324 KB
Cold denaturation of ฮฑ-lactalbumin
โœ Mineyuki Mizuguchi; Daisuke Hashimoto; Masao Sakurai; Katsutoshi Nitta ๐Ÿ“‚ Article ๐Ÿ“… 2000 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 189 KB

We have investigated the thermal unfolding of bovine โฃ-lactalbumin by means of circular dichroism spectroscopy in the far-and nearultraviolet regions, and shown that the native โฃ-lactalbumin undergoes heat and cold denaturation. The guanidine hydrochloride-induced unfolding of โฃ-lactalbumin was also

Cold Denaturation of Staphylococcal Nucl
โœ Yuri V. Griko, Peter L. Privalov, Julian M. Sturtevant and Sergey Yu. Venyaminov ๐Ÿ“‚ Article ๐Ÿ“… 1988 ๐Ÿ› National Academy of Sciences ๐ŸŒ English โš– 616 KB